Summary: F-actin capping protein, beta subunit
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "F-actin capping protein". More...
F-actin capping protein Edit Wikipedia article
| F-actin capping protein alpha subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| solution nmr structure of s100b bound to the high-affinity target peptide trtk-12 | |||||||||
| Identifiers | |||||||||
| Symbol | F-actin_cap_A | ||||||||
| Pfam | PF01267 | ||||||||
| InterPro | IPR018315 | ||||||||
| PROSITE | PDOC00609 | ||||||||
| SCOP | 1izn | ||||||||
| SUPERFAMILY | 1izn | ||||||||
|
|||||||||
| F-actin capping protein, beta subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | F_actin_cap_B | ||||||||
| Pfam | PF01115 | ||||||||
| InterPro | IPR001698 | ||||||||
| PROSITE | PDOC00203 | ||||||||
| SCOP | 1izn | ||||||||
| SUPERFAMILY | 1izn | ||||||||
|
|||||||||
In molecular biology, the F-actin capping protein is a protein which binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins.[1] The alpha subunit is a protein of about 268 to 286 amino acid residues and the beta subunit is approximately 280 amino acids , their sequences are well conserved in eukaryotic species.[2]
The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis, as well as muscle contraction.[1]
[edit] References
- ^ a b Maruyama K, Kurokawa H, Oosawa M, Shimaoka S, Yamamoto H, Ito M, Maruyama K (May 1990). "Beta-actinin is equivalent to Cap Z protein". J. Biol. Chem. 265 (15): 8712â5. PMID 2341404.
- ^ Cooper JA, Caldwell JE, Gattermeir DJ, Torres MA, Amatruda JF, Casella JF (1991). "Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ". Cell Motil. Cytoskeleton 18 (3): 204â14. doi:10.1002/cm.970180306. PMID 1711931.
This article incorporates text from the public domain Pfam and InterPro IPR018315
This article incorporates text from the public domain Pfam and InterPro IPR001698
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
F-actin capping protein, beta subunit Provide feedback
No Pfam abstract.
External database links
| PANDIT: | PF01115 |
| PROSITE: | PDOC00203 |
| Pseudofam: | PF01115 |
| SCOP: | 1izn |
| SYSTERS: | F_actin_cap_B |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001698
The WASH complex is present at the surface of endosomes and recruits and activates the Arp2/3 complex to induce actin polymerisation. The WASH complex plays a key role in the fission of tubules that serve as transport intermediates during endosome sorting [PUBMED:19922875].
The WASH complex consists of several subunits: F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 (strumpellin) and CCDC53.
The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis [PUBMED:2341404], as well as muscle contraction.
The F-actin capping protein binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin (see INTERPRO) and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins [PUBMED:2341404].
The beta subunit is a protein of about 280 amino acid residues whose sequence is well conserved in eukaryotic species [PUBMED:2179733].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| F-actin capping protein complex (GO:0008290) | |
| Molecular function | actin binding (GO:0003779) |
| Biological process | actin cytoskeleton organization (GO:0030036) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (31) |
Full (384) |
Representative proteomes | NCBI (354) |
Meta (4) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (89) |
RP35 (133) |
RP55 (198) |
RP75 (239) |
|||||
| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (31) |
Full (384) |
Representative proteomes | NCBI (354) |
Meta (4) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (89) |
RP35 (133) |
RP55 (198) |
RP75 (239) |
|||||
| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 31 |
| Number in full: | 384 |
| Average length of the domain: | 220.90 aa |
| Average identity of full alignment: | 55 % |
| Average coverage of the sequence by the domain: | 84.34 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 242 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the F_actin_cap_B domain has been found. There are 28 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence